Coevolving residues inform protein dynamics profiles and disease susceptibility of nSNVs
Fig 4
Comparison of B-factors obtained from experiments, Seq-GNM, GNM from monomeric structure, and GNM from oligomeric structure.
B-factors are shown on the respective structures for (a) 5'(3')-deoxyribonucleotidase (2JAO) and (b) Aldehyde Dehydrogenase 7A1 (2J6L). (a) The correlation of Seq-GNM to experimental B-factors is 0.83 while correlation of GNM B-factors obtained from monomer to experimental B-factors is 0.63. When dimer a is used for GNM analysis the correlation of GNM B-factors obtained from monomer to experimental B-factors increased to 0.72. (b) The correlation of Seq-GNM to experimental B-factors is 0.61 while correlation of GNM B-factors obtained from monomer to experimental B-factors is 0.37. When a tetramer is used for GNM analysis the correlation of GNM B-factors obtained from monomer to experimental B-factors increase to 0.76. The change in correlation for GNM between monomer and oligomer clearly shows the drawback for dependence on the crystal structure of biounits. However, Seq-GNM captures the interface B-factors correctly.